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Database: UniProt
Entry: A0A3Q2W0E1_HAPBU
LinkDB: A0A3Q2W0E1_HAPBU
Original site: A0A3Q2W0E1_HAPBU 
ID   A0A3Q2W0E1_HAPBU        Unreviewed;      1009 AA.
AC   A0A3Q2W0E1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=MAN2B2 {ECO:0000313|Ensembl:ENSHBUP00000018021.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000018021.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000018021.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   RefSeq; XP_005925907.1; XM_005925845.2.
DR   AlphaFoldDB; A0A3Q2W0E1; -.
DR   STRING; 8153.ENSHBUP00000018021; -.
DR   Ensembl; ENSHBUT00000026936.1; ENSHBUP00000018021.1; ENSHBUG00000020161.1.
DR   GeneID; 102308899; -.
DR   CTD; 23324; -.
DR   GeneTree; ENSGT01030000234638; -.
DR   OMA; LWMILGS; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   CDD; cd10811; GH38N_AMII_Epman_like; 1.
DR   Gene3D; 2.60.40.1360; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF28; EPIDIDYMIS-SPECIFIC ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|RuleBase:RU361199};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           22..1009
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5018377859"
FT   DOMAIN          355..438
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1009 AA;  115784 MW;  4F8E1E3F2742B6E9 CRC64;
     MGFVAAVVFA VCCWFSHGVA GQEEPIQTFV IPHSHMDVGW VYTIQESMHA YAANVYSSVT
     EELSKVKERR FIAVEQEFFR LWWDTVASVT QKKQVRQLIK EGRLEFIIGG QVMHDEAVTD
     LDDDILQMME GHGFLYETFG VRPQFSWHVD PFGASATTPV LFALAGFNAH LISRIDYDLK
     DTMQKNKKLQ FVWRGSPSLK SQQEIFTHTM DQFSYCTPSY LPFSNRSGFY WNGVALFPDP
     PKDGIYPNMS LPVIKETVHA YAKTMVENIK QRAAWFRTHH VLWPWGCDKQ FYNSSVQFNN
     MDPLMKYINQ NSKEFGVTVQ YATLSEYFQA IYQSNLTWEV RGSEDFLPYS TEPYQAWTGF
     YASRNVLKGV ARQASSKLYA AETLFARYRI SFPDGPVAKD WALDKLRALR WAVSEVQHHD
     GITGTESPKV ADMYLQHLLQ AMMGAEELLA ALFLLPHNLM SPSTLGERYP TKADVDQALE
     QHVIVYNPLA WNITTIVNVT VTQPSAAVFD DDGQPVPAQI QGSAHSNATY DLFIVVELGG
     LQYRKYLIKF PENSKAYEAK AASFERRGVK DRAKAGRRLL PVLSECYELL FDQDTNLLHS
     ITYLEEKRRV MITQDFWEYD ANGDVKAGPI SDNYIFSANG SAVRAYKAVE MEIIPGKIVT
     EIRQYFYREE SDKDYAYSIT TRVPECFGTK LPCHRLEQTY SLGPLSLNTE VVLRTSTSVK
     NNRTLYSDDN GYQMMKRTYR KFTNNTLARN YFPMVRTAYI EDDLSRLVLV SDRAHGVSSQ
     TDGQLEVMLH RRLWNNLQWN LGYNLTLNDS SVVRPTLWMM LGSVSATSKL YQREAVQLQH
     RPVVMPIDQP QKPWQVKEPK RGSPLRSVVL PPNLHLLSLS VPGWNYCSNH SVHLSHIQSG
     KDLHSQPDYD RILLRIMHLF EEGEDPELSK PVTINLKEAL QGMGEVKGVE ERSLTGTWDV
     ASLQRWKWKT ADNLENDNKQ QRTRDDNFTV TISPKEIRTF FVHFVSRNF
//
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